A1AE52
Gene name |
hisS |
Protein name |
Histidine--tRNA ligase |
Names |
Histidyl-tRNA synthetase, HisRS |
Species |
Escherichia coli O1:K1 / APEC |
KEGG Pathway |
ecv:APECO1_4010 |
EC number |
6.1.1.21: Ligases forming aminoacyl-tRNA and related compounds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A1AE52
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1AE52-F1 | Predicted | AlphaFoldDB |
No variants for A1AE52
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1AE52 | |||||
No associated diseases with A1AE52
4 regional properties for A1AE52
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.21 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| histidine-tRNA ligase activity | Catalysis of the reaction: ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| histidyl-tRNA aminoacylation | The process of coupling histidine to histidyl-tRNA, catalyzed by histidyl-tRNA synthetase. The histidyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3''-OH group of a histidine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKNIQAIRG | MNDYLPGETA | IWQRIEGTLK | NVLGSYGYSE | IRLPIVEQTP | LFKRAIGEVT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DVVEKEMYTF | EDRNGDSLTL | RPEGTAGCVR | AGIEHGLLYN | QEQRLWYIGP | MFRHERPQKG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RYRQFHQLGC | EVFGLQGPDI | DAELIMLTAR | WWRALGISEH | VTLELNSIGS | LEARANYRDA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LVAFLEQHKE | KLDEDCKRRM | YTNPLRVLDS | KNPEVQALLN | DAPALGDYLD | EESREHFAGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CKLLESAGIA | YTVNQRLVRG | LDYYNRTVFE | WVTNSLGSQG | TVCAGGRYDG | LVEQLGGRAT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PAVGFAMGLE | RLVLLVQAVN | PEFKADPVVD | IYLVASGADT | QSAAMALAER | LRDELPGVKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MTNHGGGNFK | KQFARADKWG | ARVAVVLGES | EVANGTAVVK | DLRSGEQTAV | AQDSVAAHLR |
| TLLG |